Purification and characterization of an extradiol dioxygenase which preferentially acts on 4-methylcatechol
DC Field | Value | Language |
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dc.contributor.author | Ha, YM | - |
dc.contributor.author | Jung, YH | - |
dc.contributor.author | Kwon, DY | - |
dc.contributor.author | Kim, YC | - |
dc.contributor.author | Kim, Y | - |
dc.contributor.author | Kim, CK | - |
dc.contributor.author | Min, KH | - |
dc.date.available | 2021-02-22T16:48:07Z | - |
dc.date.issued | 1999-06 | - |
dc.identifier.issn | 1017-7825 | - |
dc.identifier.issn | 1738-8872 | - |
dc.identifier.uri | https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/16838 | - |
dc.description.abstract | A catechol 2,3-dioxygenase (C230) was purified to apparent homogeneity from Pseudomonas putida SU10 through several purification steps consisting of ammonium sulfate precipitation and chromatographies on DEAE 5PW, Superdex S-200, and Resource-Q. Gel filtration indicated a molecular mass under nondenaturing conditions of about 130 kDa. The enzyme has a subunit of 34 kDa as was determined by SDS-PAGE. These results suggest that the native enzyme is composed of four identical subunits. The N-terminal amino acid sequence (30 residues) of the enzyme has been determined and exhibits high identity with other extradiol dioxygenases. The reactivity of this enzyme towards catechol and methyl-substituted catechols is somewhat different from that seen for other catechol 2,3-dioxygenases, with 4-methylcatechol cleaved at a higher rate than catechol or 3-methylcatechol. K-m values of the enzyme for these substrates are between 3.5 and 5.7 M. | - |
dc.format.extent | 6 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | SPRINGER-VERLAG SINGAPORE PTE LTD | - |
dc.title | Purification and characterization of an extradiol dioxygenase which preferentially acts on 4-methylcatechol | - |
dc.type | Article | - |
dc.publisher.location | 싱가폴 | - |
dc.identifier.scopusid | 2-s2.0-0344348904 | - |
dc.identifier.wosid | 000081304400003 | - |
dc.identifier.bibliographicCitation | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.9, no.3, pp 249 - 254 | - |
dc.citation.title | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY | - |
dc.citation.volume | 9 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 249 | - |
dc.citation.endPage | 254 | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalResearchArea | Microbiology | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.subject.keywordPlus | PSEUDOMONAS-PUTIDA MT-2 | - |
dc.subject.keywordPlus | CATECHOL 2,3-DIOXYGENASE | - |
dc.subject.keywordPlus | NUCLEOTIDE-SEQUENCE | - |
dc.subject.keywordPlus | SUBSTRATE-SPECIFICITY | - |
dc.subject.keywordPlus | TOL PLASMID | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordPlus | METAPYROCATECHASE | - |
dc.subject.keywordPlus | PWWO | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | CATABOLISM | - |
dc.subject.keywordAuthor | catechol 2,3-dioxygenase | - |
dc.subject.keywordAuthor | substrate specificity | - |
dc.subject.keywordAuthor | N-terminal sequence | - |
dc.subject.keywordAuthor | kinetic studies | - |
dc.subject.keywordAuthor | Pseudomonas putida SU10 | - |
dc.identifier.url | https://kiss.kstudy.com/Detail/Ar?key=284625 | - |
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